Browse by author
Lookup NU author(s): Lorand Szabo, Tibor Nagy, Emeritus Professor Harry Gilbert
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
Plant cell wall hydrolases generally have a modular structure consisting of a catalytic domain linked to one or more noncatalytic carbohydrate-binding modules (CBMs), whose common function is to attach the enzyme to the polymeric substrate. Xylanase A from Pseudomonas fluorescens subsp. cellulosa (Pf Xyn10A) consists of a family 10 catalytic domain, an N-terminal family IIa cellulose-binding module, and an internal family 10 cellulose-binding module. The structure of the 45-residue family 10 CBM has been determined in solution using NMR. It consists of two antiparallel β-sheets, one with two strands and one with three, with a short α-helix across one face of the three-stranded sheet. There is a high density of aromatic residues on one side of the protein, including three aromatic residues (Tyr8, Trp22, and Trp24), which are exposed and form a flat surface on one face, in a classical polysaccharide-binding arrangement. The fold is closely similar to that of the oligonucleotide/oligosaccharide-binding (OB) fold, but appears to have arisen by convergent evolution, because there is no sequence similarity, and the presumed binding sites are on different faces.
Author(s): Raghothama S, Simpson PJ, Szabo L, Nagy T, Gilbert HJ, Williamson MP
Publication type: Article
Publication status: Published
Journal: Biochemistry
Year: 2000
Volume: 39
Issue: 5
Pages: 978-984
ISSN (print): 0006-2960
ISSN (electronic): 1520-4995
Publisher: American Chemical Society
URL: http://dx.doi.org/10.1021/bi992163+
DOI: 10.1021/bi992163+
PubMed id: 10653641
Altmetrics provided by Altmetric
